The separation of apolipoprotein D from cholesteryl ester transfer protein.
This study addresses the question of whether cholesteryl ester transfer protein and apolipoprotein D are identical. The data presented show that these two proteins do not co-purify during hydrophobic and cationic exchange chromatography and are readily separated by molecular sieve chromatography or electrophoresis. Furthermore, the precipitation of apolipoprotein D by specific antisera did not diminish the transfer activity of lipoprotein-deficient plasma. We conclude that apolipoprotein D and cholesteryl ester transfer protein have significantly different physicochemical properties.
D000818:Animals; D001053:Apolipoproteins / Q000097:blood / Q000302:isolation & purification*; D053399:Apolipoproteins D; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D053480:Cholesterol Ester Transfer Proteins; D002788:Cholesterol Esters / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins; D007118:Immunoassay; D005779:Immunodiffusion; D007136:Immunoglobulins; D011817:Rabbits
D001053:Apolipoproteins; D053399:Apolipoproteins D; D002352:Carrier Proteins; D053480:Cholesterol Ester Transfer Proteins; D002788:Cholesterol Esters; D006023:Glycoproteins; D007136:Immunoglobulins